Final Exam review Flashcards
Forms of an element with different numbers of neutrons, and thus different mass numbers
Isotopes
Particles with negative charge that determine the charge of an atom
Electron
four most common elements in living organisms
Carbon, Oxygen, Nitrogen, Hydrogen
The smallest unit of matter that retains all chemical properties of an element
Atom
Particles with positive charge that identify the element.
Protons
Proton, Neutron, Electron
Sub-atomic particles
Particles with neutral charge that contribute to an atom’s mass
Neutron
The outermost shell of an atom that determines its behavior
Valance Shell
Substances used at the beginning of a reaction
Reactants
Substances formed at the end of a reaction
products
The attractive force that links atoms together to form molecules
Chemical Bonds
Bonds where electrons are shared between atoms
Covalent Bonds
Bonds where atoms give up or gain electrons
Ionic Bond
The positive charge of hydrogen in a water molecule bonds/is attracted to the negative oxygen from a different water molecule
Hydrogen Bond
The liquid that dissolves other things
Solvent
What gets dissolved (sugar)
Solute
Water molecules at the liquid-gas interface stick together due to hydrogen bonding
Cohesion
The capacity of a substance to withstand being ruptured when placed under tension or stress
Surface Tension
Determined by the pH (percent hydrogen) of a solution indicated
Acidity or Alkalinity
Attraction between water molecules and other molecules
Adhesion
Has more hydrogens
Higher in Acidity
Key Component of Macromolecules
Carbon
Molecules consisting of carbon and hydrogen
Hydrocarbons
Molecules that have the same chemical formula but differ in placement/arrangement of atoms or types of bonds between atoms
Isomer
Isomers that have a different covalent arrangement of atoms
Structural Isomers
Isomers that have a different arrangement of atoms around a double bond
Geometric Isomers
Molecules that share chemical formula and bonds but differ in 3D placement of atoms; mirror images
Enantiomers
Groups of atoms within a molecule that confer consistent specific properties to these molecules
Functional Groups
functional group with an oxygen and a hydrogen atom
Hydroxyl
A functional group with a nitrogen atom bonded to two hydrogen atoms
Amino
A functional group with a phosphorus atom bonded to four oxygen atoms
Phosphate
Carbohydrates, Lipids, Proteins, Nucleic Acid
Major Classes of Macromolecules
Individual sub-units that macromolecules consist of
Monomers
Monomers that are linked together via covalent bonds
Polymers
The process where two molecules of glucose are linked to form the disaccharide maltose
Dehydration Synthesis
The process of breaking polymers down into individual monomers - also known as a dehydration reaction
Hydrolysis
Biological molecules that catalyze or ‘speed up’ reactions
Enzymes
Found in grains, fruits, and vegetables. Provide energy to the body in the form of glucose
Carbohydrates
Monosaccharides, Disaccharides, Polysaccharides
Three Main Carbohydrate Subtypes
Carbohydrates with 3-7 carbons
Monosaccharides
A monosaccharide with six carbons
Glucose
CH2O
Sugar Formula
Disaccharides are formed when two monomers are joined by a dehydration synthesis
Glycosidic Bond
Are created by Glycosidic
Linkages Maltose, Lactose, and Sucrose
Non-polar
Polarity of Lipids
Glycerol and Fatty Acids
Two main components of Fats
Formed by three fatty acids joining a glycerol backbone
Triglycerol
Molecules with two fatty acids and a modified phosphate group attached to a glycerol backbone
Phospholipids
Includes a head followed by a tail.
Phospholipid Bilayer
Molecules with four linked carbon rings
Steroids
steroid with four rings
Cholesterol
Catalysts in biochemical reactions
Enzyme
A diverse range of function
Protein
The monomers that make up proteins
Amino Acids
Amino acid monomers are linked via peptide bond formation (dehydration synthesis reaction
Peptide Bond
Based upon four levels of structure
Protein Shape
DNA and RNA
Two Types of Nucleic Acid
Primarily involved in protein synthesis
RNA
DNA and RNA Monomers
Nucleotides
Nucleotides’ three parts are:
Nitrogenous base, Pentose sugar, and One or more phosphate groups
Stronger than a light microscope
Electron microscope
four common components of cells
Cytoplasm, Plasma membrane, DNA, Ribosomes
Lack membrane-enclosed organelles
Prokaryotes
Lacks in prokaryotes
Nucleus
Location of DNA in prokaryotes
Nucleoid
Perforate the nuclear envelope membrane
Nuclear pores
Site for conversion of stored energy (ATP)
Mitochondria
Contain digestive enzymes
Lysosomes
Mitochondria and chloroplasts originated as independent prokaryotic organisms, are the ancestors of eukaryotic cells
Endosymbiosis hypothesis
Internal membranes and organelles that modify, package, and transport lipids and proteins
Endomembrane System
Modifies proteins and synthesizes lipids
Endoplasmic reticulum (ER)
Ribosomes attach to create proteins (rough ribos)
Rough Endoplasmic reticulum
Synthesizes carbohydrates, lipids, steroid hormones, and stores Ca++ (smooth like butter)
Smooth Endoplasmic Reticulum
Transports lipids or proteins in vesicles to be stored, packaged, and tagged (amazon of cell)
Golgi Apparatus
Highways of cells and helps maintain the shape of cells
Cytoskeleton
Hairs on the cell
Cilia
Tails that move the cell (sperm lookin)
Flagella
plasmodesmata, tight junctions, desmosomes, gap junctions
types of intercellular junctions
Provide direct channels of communication between cells
Intercellular Junctions
Cytoplasm connecting channels that allow materials to move from cell to cell
Plasmodesmata
Watertight seals that prevent materials from leaking
Tight junctions
Short proteins in the plasma membrane that act as spot welds
Desmosomes
Protein-lined pores that allow water and small molecules to pass
Gap junctions
All chemical reactions of a cell or organism
Metabolism
Small molecules are assembled into large ones, energy is required
Anabolic
Large molecules are broken down into small ones, energy is released
Catabolic
Energy of objects in motion
Kinetic energy
Energy of objects that have the potential to move
Potential energy
Amount of energy available to do work
Gibb’s Free Energy (G)
the reaction will happen no matter if I put energy into it
negative G value
energy is needed for reaction
positive G value
Energy required for a reaction to proceed
Activation Energy
Protein catalysts that speed up reactions by lowering the required activation energy
Enzymes
Molecules that interact at the enzyme’s active site
Substrate
where the substrate and enzyme interact and react
active site
Mild shift in shape at the active site that optimizes reactions
Induced Fit
Modify the active site of the enzyme to reduce or prevent substrate binding
Allosteric inhibitors
Modify the active site of the enzyme to increase substrate affinity
Allosteric activators
Have a similar shape to the substrate, competing for the active site
Competitive inhibitors
Bind to the enzyme at a different location, causing a slower reaction rate
Noncompetitive inhibitors
End product of a pathway inhibits an upstream step
Feedback inhibition
Defining outer border, managing what enters and exits the cell, receiving external signals, adhering to neighboring cells
Plasma Membrane Functions
Main fabric of the plasma membrane composed of an amphiphilic lipid molecule
Phospholipids
Proteins that go through the membrane
Integral Proteins
Proteins on the side of the membrane, inside or out, never through
Peripheral Protein
Affected by phospholipid type, temperature, and cholesterol
Fluidity
Allows some molecules to pass through, but not others
Selective Permeability
Diffusion of substances down their concentration gradient (from high concentration to low)
Passive transport
Greater difference results in faster diffusion
Concentration gradients
Moves substances down their concentration gradients through transmembrane proteins
Facilitated transport
Diffusion of water across a membrane
Osmosis
Describes how extracellular solutions can change the volume of a cell by affecting osmosis
Tonicity
Extracellular fluid has lower osmolarity than the cytosol - water leaves the cell (shrivels)
Hypotonic
Extracellular fluid has the same osmolarity as the cytosol - water does not move (normal)
Isotonic
Extracellular fluid has higher osmolarity than the cytosol - water enters the cell(busts)
Hypertonic
Transport of ions or molecules against their concentration or electromagnetic gradient
Active Transport
Uses energy from ATP hydrolysis to move ions or molecules up their concentration gradient
Primary active transport
Uses an electrochemical gradient to move a different substance against its concentration gradient
Secondary active transport
Cytoplasm contains more negatively charged molecules than the extracellular fluid
Electrochemical Gradients
Does not require energy or ATP
Passive transport
Requires energy or ATP
Active transport
Carries one molecule or ion
Uniporter
Carries two different molecules or ions in the same direction
Symporter
Carries two different molecules or ions in different directions
Antiporter
Occurs when cells need to import or export large molecules/particles
Bulk Transport
bulk transport requires..
energy
Process of bringing substances into the cell
Endocytosis
Cell membrane surrounds a particle and engulfs it (cellular eating)
Phagocytosis
Cell membrane invaginates, surrounds a small volume of fluid, and pinches off (cellular drinking)
Pinocytosis
Uptake of a specific substance targeted by binding to receptors on the membrane
Receptor mediated endocytosis
Vesicles containing substances fuse with the plasma membrane and release contents to the exterior of the cell (exit)
Exocytosis
When a molecule gains an H, (xH)
Reduction
When a molecule loses an H, it has been oxidized (+)
Oxidation
Carries 2e- and 1H+ more than NAD
NADH
Result of a redox reaction
FADH and NADPH
Process of adding a phosphate group to a molecule, producing energy
Phosphorylation
Metabolic pathway that occurs in the cytosol, does not require oxygen
Glycolysis
Occurs when there is no or not enough oxygen in the cell
Fermentation
Occurs when there is oxygen in the cell
Cellular respiration
Outcome of glycolysis
Pyruvate
Result of the oxidation of pyruvate
Acetyl CoA
Metabolic pathway that results in reduced molecules and oxaloacetate
Citric Acid Cycle
Involves electrons, electron carriers, protons, and oxygen
Oxidative Phosphorylation
Allow electrons to pass through
Electron carriers
Final electron acceptor in Oxidative Phosphorylation
Oxygen
Found in the intermembrane space, move down the electron gradient to create ATP
Protons
Macromolecules that can be broken down
Lipids, Fats, and Proteins
Converts light energy to chemical energy, occurs in the thylakoid membrane
Light reaction
Location where light reaction occurs
Thylakoid membrane
Occurs in the stroma of chloroplasts, fixes carbon
Calvin Cycle
Main pigments of thylakoid membranes
Chlorophylls
Type of carotenoid, main pigment of thylakoid membranes
Carotene
Capture light for photosynthesis
chlorophyll a, chlorophyll b and carotenoids
Require water and light
Photosystems
Molecule necessary for carbon fixation in the Calvin Cycle
RuBP
Process that requires carbon, occurs in the Calvin Cycle
Carbon fixation
Goal of the Calvin Cycle, a three-carbon sugar
G3P
Signals move by diffusion through extracellular matrix
Paracrine signaling
Signals distant cells, produce a slower response with long-lasting effect
Endocrine signaling
Signals cells that can also bind to the released ligand
Autocrine signaling
Allows small signaling molecules to move between cells
Direct signaling across gap junctions
Gated ion channels that open when the signaling molecule binds
Ion channel-linked receptors
Trigger a cellular response when the signaling molecule binds
G-protein-linked receptors
Receptor tyrosine kinase, triggers a cellular response
Enzyme-linked receptors
Transmission of a signal through the cell membrane and into the cytoplasm
Signal transduction
Two receptors bind to each other to form a stable complex
Dimerization
Chain of events that follow ligand binding to a receptor
Signaling pathway
Signals from different receptors merge to activate the same response
Signal integration
Enzyme that catalyzes the transfer of a phosphate group (kind enough to lend Ph)
Kinase
Series of steps where kinase is given phosphate, creating an activation cascade
Phosphorylation Cascade
Small molecules that propagate a signal after binding of the signaling molecule to the receptor
Second Messengers
Cell death, termination of cell signals
Apoptosis
23 of them, Contain DNA, x and y
Chromosomes
have 2 matched sets of chromosomes (diploid)
somatic cells
have half the number of chromosomes (haploid)
gametes
Structure of DNA
DNA double helix
DNA wraps around histone protein
Histone protein
Coiling of DNA and histone protein
Nucleosome
Further condensation of nucleosome
Chromatin fiber
Result of DNA synthesis
Duplicated chromosomes
Includes mitosis and cytokinesis (can tell by looking)
Mitotic Phase
synthesis phase, doubling of DNA
S DNA
growth phases
G1 and G2
Nuclear division
Mitosis
Chromosomes condense, nuclear envelope breaks down
Prophase
Chromosomes line up along metaphase plate
Metaphase
Chromatids become separated and pulled apart
anaphase
Chromosomes reach opposite poles and begin to decondense
Telophase
Completes cell division via physical separation of cytoplasmic components
Cytokinesis
Control points in the cell cycle at G1, G2, and metaphase of mitosis
Regulated internal checkpoints
Promote movement to the next step of the cell cycle
Positive regulators
Stop the advancement of the cell cycle
Negative regulators
Positive regulators of the cell cycle
Cyclins and Cyclin-dependent kinase (Cdks)
Negative regulators of the cell cycle
Retinoblastoma protein (Rb), p53, p21
Considered the father of genetics
Gregor Medel
Result of true breeding
Parent generation (P)
First filial generation from a cross between siblings (brother and sister)
F1 hybrid
Second filial generation produced by crossing 2 F1 individuals
F2
Succeeding generation after F2 (stabalized)
F3, F4, and F5
Characteristic version of a trait that is observable (blue eyes)
Phenotype
Specific versions of a gene
Alleles
Alleles that mask others, often designated with capital letters
Dominant
Specific combination of alleles that determines the phenotype
Genotype
Alleles that are masked by others, often designated with lowercase letters
Recessive
Individual with both alleles for the same trait being the same (PP - are true breeding)
Homozygote
Individual with alleles for the same trait being different (Pp - are non-true breeding)
Heterozygote
place of interest on a chromosome, usually a gene
locus
the most common allele in a population (normal allele)
wildtype allele
a rare allele in a population. reasoned to be the most recently formed allele by mutation (non-normal allele)
mutant allele
can be used to make genetic inferences
pedigree
Situation in which one allele is not completely dominant over another allele (shared dominance, mixed phenotypes)
incomplete dominance
using a virus as a syringe to do experiements
bacteriophages
was a part of the team that discovered the structure of the DNA helix (along w/ Watson and Crick)
Rosalind Franklin
three different parts:
sugar, nitrogenous base, and phosphate group
Each nucleiotide is made up of-
carbon one, carbon three, carbon five
the three important carbons
has the nitrogenous base
carbon one
hydroxl group, where reaction occurs with new nucleiotides
carbon three
ALWAYS attatches the the phosphate group
carbon five
3’ end
which end do nucleotides attatch to
5’ to 3’
direction of DNA
is formed when helicase separates the DNA strand at the orign of replication
replication fork
the enzyme the unzips (separetes top and bottom strands) DNA
helicase
Synthesizes RNA primers needed to start replication
primase
prevents the overwidening of the DNA strands (removes tension)
tomoisomerase
bind to the single strand of DNA tp prevent the helix from refomring (keeps the strantds open)
Single-strand binding proteins
synthesizes new DNA on the leading strand
DNA polymerase iii
bacckfilled with RNA primer
the lagging strand gets-
is added to the ends of DNA strands to protect and maintain DNA
Telomerase enzyme
seals the gaps between DNA (okazaki fragmants)
DNA ligase
replaces RNA primer with DNA
DNA polymerase i
has no effect on the protein sequence
silent mutations
result in an amino acid substitution
missense mutation
substitues a stop codon for an amino acid (confusing)
nonsene mutation
may result in a whole shift in the reading frame or insertion of a stop codon
frameshift mutations
DNA is first transcribed into mRNA, then mRNA is translated into proteins
central dogma
promoter (piece of upstream DNA) indicates where the RNA polymerase should bind to begin process
transcription initiation
RNA polymerase adds complimentary nucleotides (ACUG) to make mRNA
transcription elongation
include anticodons which attach to corresponding codons
tRNA (transfer RNA)
mRNA attaches to the smaller subunit of a ribosome
translation initiation
tRNA move into the appropriate amino acid in groups of three, to code into the correct protein, and the chain of proteins grows
translation elongation
are within the ribosome structure, mRNA moves through the order of A-P-E
E-P-A sites
mRNA enters and confirms the match
A-site
for making polypeptides, the ribosome attaches to the existing chain
P-site
where the codon ejects and binds to a specific structure
E-site
the ribosome reaches a STOP codon, the ribisome breaks and releases the mRNA
translation termination
